Bio 21 Cell Biology

List of Terms and Study Guide 2

for Exam 1 on 2/19

 

ligand

affinity

thermally induced motion

equilibrium

association vs dissociation

enzyme

active site

substrate

transition state

activation energy

stable conformation

small organic molecules as co-factors

allosteric regulation

allosteric enzyme

allosteric modulator

allosteric site

feedback inhibition

competitive inhibitor

non-competitive inhibibitor

allosteric inhibitor

allosteric activator

cooperative binding

KM

Vmax

Michaelis-Menten equation (know what it is, don't memorize it)

turnover number

protein phosphorylation

Ser, Thr, Tyr

ATP

protein kinase

protein phosphatase

GTP-binding protein

 

carbohydrate

(CH2O)n

monosaccharide

disaccharide

oligosaccharide

polysaccharide

glycogen

starch

cellulose

glycosylation

glycoprotein

glycolipid

dehydration synthesis

hydrolysis

 

fatty acid

CH3(CH2)nCOOH

hydrocarbon chain/tail

saturated

unsaturated

triacylglycerol

phospholipid

lipid bilayer

amphipathic

 

nucleotide

nucleic acid

DNA

RNA

G,A,T,C

base pair

ATP

GTP

 

1. Understand how proteins are able to bind specifically to their ligands and that a protein's function is largely determined by the molecules with which it can bind and interact.

2. Understand how enzymes are able to catalyze reactions (be familiar with the general ways in which an enzyme can speed up a reaction, such as lowering activation energy by stabilizing transition states).

3. Understand the relationship between Km, Vmax and substrate affinity. Be able to determine Vmax and Km from a graph of enzyme activity vs substrate concentration. Understand that various types of regulation (such as an allosteric modulator or phosphorylation state) can alter an enzyme's affinity for its substrate and thus alter its Km. Understand how such changes in Km affect an enzyme's activity (i.e., the rate at which it can catalyze a reaction).

4. Understand the difference between a competitive and non-competitive inhibitor and the general mechanism whereby each is able to decrease the activity of a targeted enzyme.

5. Know how the product of a set of reactions, such as in a biosynthetic pathway, can function as an allosteric inhibitor to regulate production of itself by a negative feedback loop.

6. Be able to recognize the general chemical structure of a carbohydrate.

7. Be able to show how two sugar subunits can be joined by a condensation reaction. Be able to show how multiple sugar subunits can be joined together to form complex branching molecules. Be able to show how the reverse reaction (hydrolysis) can break a sugar into smaller subunits.

8. Know the various ways by which cell's utilize carbohydrates.

9. Be able to recognize the general chemical structure of a fatty acid. Be able to distinguish between saturated and unsaturated fats.

10. Be able to recognize a phospholipid. Be able to label the hydrophilic head and the hydrophobic tail regions. Understand the amphipathic nature of a fatty acid and of a phospholipid. Understand the behavior of these amphipathic molecules in an aqueous solution and how this behavior can lead to the formation of a lipid bilayer.

11. Be able to recognize the chemical structure of a nucleotide. Know how nucleotides can be joined together to form larger macromolecules such as DNA and RNA. Know the names of the four nucleotides that form the base pairs of DNA.

12. Be able to recognize the ATP molecule. Know which class of organic molecule to which it belongs. Understand the role of ATP in protein phosphorylation.

13. Understand the role of GTP in regulating the activity of GTP-binding proteins.

14. For the various regulatory mechanisms that control the activity of a protein: Know how the protein can be activated and know how it can be "shut off".